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P13933 (GUN1_STRSS) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase 1

EC=3.2.1.4
Alternative name(s):
CMCase I
Carboxymethyl cellulase
Cellulase
Endo-1,4-beta-glucanase
Gene names
Name:casA
OrganismStreptomyces sp. (strain KSM-9)
Taxonomic identifier74575 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

CMCase I preferentially hydrolyzes carboxymethyl cellulose (CMC).

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sequence similarities

Belongs to the glycosyl hydrolase 6 (cellulase B) family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.5.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ?
Propeptide? – 70PRO_0000007907
Chain71 – 359289Endoglucanase 1
PRO_0000007908

Sites

Active site1541 By similarity
Active site1921Proton donor By similarity
Active site3391Nucleophile By similarity

Amino acid modifications

Disulfide bond155 ↔ 199 By similarity

Sequences

Sequence LengthMass (Da)Tools
P13933 [UniParc].

Last modified June 1, 1994. Version 3.
Checksum: F1300238834E906C

FASTA35936,515
        10         20         30         40         50         60 
MENPRTTPTP TPLRRRRSER RARGGRVLTA LTGVTLLAGL AIAPAATGAS PSPAPPASPA 

        70         80         90        100        110        120 
PSADSGTADA GTTALPSMEL YRAEAGVHAW LDANPGDHRA PLIAERIGSQ PQAVWFAGAY 

       130        140        150        160        170        180 
NPGTITQQVA EVTSAAAAAG QLPVVVPYMI PFRDCGNHSG GGAPSFAAYA EWSGLFAAGL 

       190        200        210        220        230        240 
GSEPVVVVLE PDAIPLIDCL DNQQRAERLA ALAGLAEAVT DANPEARVYY DVGHSAWHAP 

       250        260        270        280        290        300 
AAIAPTLVEA GILEHGAGIA TNISNYRTTT DETAYASAVI AELGGGLGAV VDTSRNGNGP 

       310        320        330        340        350 
LGSEWCDPPG RLVGNNPTVN PGVPGVDAFL WIKLPGELDG CDGPVGSFSP AKAYELAGG 

« Hide

References

[1]"Cloning and nucleotide sequence of a cellulase gene, casA, from an alkalophilic Streptomyces strain."
Nakai R., Horinouchi S., Beppu T.
Gene 65:229-238(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 71-95.
[2]"Endoglucanase CasA from alkalophilic Streptomyces strain KSM-9 is a typical member of family B of beta-1,4-glucanases."
Damude H.G., Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.
Gene 123:105-107(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
[3]"Structural and functional relationships in two families of beta-1,4-glycanases."
Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A., Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.
Eur. J. Biochem. 202:367-377(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 185-222, SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L03218 Genomic DNA. Translation: AAA26713.1.
X61008 Genomic DNA. Translation: CAA43330.1.
M20921 Genomic DNA. Translation: AAA26776.1. Sequence problems.
PIRJN0544.
JT0308.

3D structure databases

ProteinModelPortalP13933.
SMRP13933. Positions 89-358.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.40. 1 hit.
InterProIPR016288. Beta_cellobiohydrolase.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamPF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSPR00733. GLHYDRLASE6.
SUPFAMSSF51989. SSF51989. 1 hit.
PROSITEPS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN1_STRSS
AccessionPrimary (citable) accession number: P13933
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 1, 1994
Last modified: October 16, 2013
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries